DAPE_MYCS2
ID DAPE_MYCS2 Reviewed; 355 AA.
AC A0R2G4;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Succinyl-diaminopimelate desuccinylase;
DE Short=SDAP desuccinylase;
DE EC=3.5.1.18;
DE AltName: Full=N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase;
GN Name=dapE; OrderedLocusNames=MSMEI_4975;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=16381882; DOI=10.1093/nar/gkj060;
RA Perrodou E., Deshayes C., Muller J., Schaeffer C., Van Dorsselaer A.,
RA Ripp R., Poch O., Reyrat J.M., Lecompte O.;
RT "ICDS database: interrupted CoDing sequences in prokaryotic genomes.";
RL Nucleic Acids Res. 34:D338-D343(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=8932306; DOI=10.1128/jb.178.22.6496-6507.1996;
RA Pavelka M.S. Jr., Jacobs W.R. Jr.;
RT "Biosynthesis of diaminopimelate, the precursor of lysine and a component
RT of peptidoglycan, is an essential function of Mycobacterium smegmatis.";
RL J. Bacteriol. 178:6496-6507(1996).
CC -!- FUNCTION: Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic
CC acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP),
CC an intermediate involved in the bacterial biosynthesis of lysine and
CC meso-diaminopimelic acid, an essential component of bacterial cell
CC walls. {ECO:0000269|PubMed:8932306}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-succinyl-(2S,6S)-2,6-diaminoheptanedioate = (2S,6S)-
CC 2,6-diaminoheptanedioate + succinate; Xref=Rhea:RHEA:22608,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:30031, ChEBI:CHEBI:57609,
CC ChEBI:CHEBI:58087; EC=3.5.1.18;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) or Co(2+) ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate
CC (succinylase route): step 3/3.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show multiple auxotrophy
CC (Met, Thr, Lys and DAP). {ECO:0000269|PubMed:8932306}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family. DapE subfamily.
CC {ECO:0000305}.
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DR EMBL; CP000480; ABK70853.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP41419.1; -; Genomic_DNA.
DR RefSeq; WP_011730316.1; NZ_SIJM01000068.1.
DR RefSeq; YP_889352.1; NC_008596.1.
DR AlphaFoldDB; A0R2G4; -.
DR SMR; A0R2G4; -.
DR STRING; 246196.MSMEI_4975; -.
DR EnsemblBacteria; ABK70853; ABK70853; MSMEG_5103.
DR EnsemblBacteria; AFP41419; AFP41419; MSMEI_4975.
DR GeneID; 66736420; -.
DR KEGG; msg:MSMEI_4975; -.
DR KEGG; msm:MSMEG_5103; -.
DR PATRIC; fig|246196.19.peg.4979; -.
DR eggNOG; COG0624; Bacteria.
DR OMA; LNSHHDT; -.
DR OrthoDB; 906744at2; -.
DR UniPathway; UPA00034; UER00021.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009014; F:succinyl-diaminopimelate desuccinylase activity; IEA:UniProtKB-EC.
DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR InterPro; IPR010174; Succinyl-DAP_deSuclase_DapE.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; SSF55031; 1.
DR TIGRFAMs; TIGR01900; dapE-gram_pos; 1.
DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cobalt; Diaminopimelate biosynthesis; Hydrolase;
KW Lysine biosynthesis; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..355
FT /note="Succinyl-diaminopimelate desuccinylase"
FT /id="PRO_0000421290"
FT ACT_SITE 72
FT /evidence="ECO:0000250"
FT ACT_SITE 126
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 331
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 355 AA; 37432 MW; FC2FF80FB3060F4C CRC64;
MGLDLSADPI ALTAALVDIP SVSRDERRIA DEIEAALRAQ APHFEVIRNG DAVLARTNLG
RPSRVMLAGH IDTVPIADNL PSRIVDGEMY GCGTSDMKAG DAVFLHLAAT ITEPTHDITL
VMYDCEEIES SANGLGRIER ELRDWLTADV AILGEPSGGY IEAGCQGTIR VVISAKGTRA
HSARSWLGDN AIHKLAPVLD RLASYQARSV DIDGCVYREG LSAVRIDGGI AGNVIPDAAS
VTVNFRFAPD RDVDQAVAHV HEVFDGLDVT LELTDAAAGA LPGLTQPAAA ALVAAAGGQV
RAKYGWTDVA RFAALGIPAV NYGPGDPNLA HRVDERVQVA AITAAADMLR TYLTT
